is structural information a must in intermolecular binding affinity calculation

Structural information is typically important in intermolecular binding affinity calculations. This is because the binding affinity between two molecules, such as a ligand and a protein, is influenced by their specific interactions and structural features. These interactions can include hydrogen bonding, electrostatic interactions, hydrophobic interactions, and others. Understanding the structural details of the binding site and the ligand can help in predicting and quantifying these interactions, which in turn, can be used to estimate the binding affinity.

Structural information is often obtained from experimental techniques such as X-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy, which provide the three-dimensional structure of the complex. Computational methods, such as molecular docking or molecular dynamics simulations, can also be used to predict the binding mode and estimate the binding affinity based on structural information.

While it is possible to estimate binding affinity without explicit structural information, the accuracy and reliability of the predictions may be limited. Structural information allows for a more detailed understanding of the molecular interactions involved in binding, which can lead to more accurate and reliable predictions of binding affinity. Therefore, in most cases, having structural information is beneficial and recommended for intermolecular binding affinity calculations.